Structural studies of three IgG kappa proteins from a patient with multiple myeloma.
Three distinct IgG proteins of similar concentration and the same light-chain type were demonstrated in a myeloma serum. The bonds between the heavy and light chains were split, and the isolated gamma- and kappa-chains were characterized by crossed immunoelectrophoresis, subgroup determination and N-terminal amino acid sequence. The studies showed that the IgG heterogeneity was due to differences in the primary structure of the variable parts of the kappa-chains. Two of the kappa-chains belonged to subgroup V kappa I, and one chain, the most anodic one, belonged to V kappa III The gamma-chains were homogeneous and belonged to subgroup VHIII.
D000368:Aged; D000595:Amino Acid Sequence; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D006801:Humans; D007123:Immunoelectrophoresis, Two-Dimensional; D007074:Immunoglobulin G / Q000302:isolation & purification; D007147:Immunoglobulin Light Chains; D007142:Immunoglobulin gamma-Chains / Q000302:isolation & purification; D007145:Immunoglobulin kappa-Chains / Q000302:isolation & purification; D008297:Male; D009101:Multiple Myeloma / Q000276:immunology*
D007074:Immunoglobulin G; D007147:Immunoglobulin Light Chains; D007142:Immunoglobulin gamma-Chains; D007145:Immunoglobulin kappa-Chains